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P67870 (CSK2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Casein kinase II subunit beta

Short name=CK II beta
Alternative name(s):
Phosvitin
Protein G5a
Gene names
Name:CSNK2B
Synonyms:CK2N, G5A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates in Wnt signaling By similarity. Plays a complex role in regulating the basal catalytic activity of the alpha subunit. Ref.16 Ref.19

Subunit structure

Tetramer composed of an alpha subunit, an alpha' subunit and two beta subunits. The beta subunit dimerization is mediated by zinc ions. Interacts with TCTEX1D3 By similarity. Interacts with CD163. Also component of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, the complex associating following UV irradiation. Interacts with MUSK; mediates phosphorylation of MUSK by CK2. Interacts with FGF1; this interaction is increased in the presence of FIBP, suggesting a possible cooperative interaction between CSNKB and FIBP in binding to FGF1. Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.27 Ref.28

Post-translational modification

Phosphorylated by alpha subunit. Ref.14 Ref.28

Sequence similarities

Belongs to the casein kinase 2 subunit beta family.

Sequence caution

The sequence CAI18393.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processWnt signaling pathway
   LigandMetal-binding
Zinc
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

adiponectin-activated signaling pathway

Inferred from direct assay PubMed 19233263. Source: BHF-UCL

axon guidance

Traceable author statement. Source: Reactome

cellular protein complex assembly

Non-traceable author statement PubMed 19324893. Source: BHF-UCL

endothelial tube morphogenesis

Inferred from mutant phenotype PubMed 19592636. Source: BHF-UCL

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of blood vessel endothelial cell migration

Inferred from direct assay PubMed 19592636. Source: BHF-UCL

negative regulation of cell proliferation

Traceable author statement PubMed 19324893. Source: BHF-UCL

positive regulation of activin receptor signaling pathway

Inferred from mutant phenotype PubMed 19592636. Source: BHF-UCL

positive regulation of pathway-restricted SMAD protein phosphorylation

Inferred from direct assay PubMed 19592636. Source: BHF-UCL

protein phosphorylation

Traceable author statement Ref.4. Source: GOC

regulation of DNA binding

Non-traceable author statement PubMed 19324893. Source: BHF-UCL

regulation of protein kinase activity

Non-traceable author statement Ref.1. Source: GOC

signal transduction

Traceable author statement Ref.3. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 19233263. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

nucleus

Inferred from direct assay PubMed 21282530. Source: UniProtKB

protein kinase CK2 complex

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionidentical protein binding

Inferred from physical interaction PubMed 10094392PubMed 14667819PubMed 21282530PubMed 21988832PubMed 23555304. Source: IntAct

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 10094392Ref.28PubMed 12769847PubMed 14667819PubMed 16977309PubMed 19011756PubMed 20664522PubMed 21078624PubMed 21282530PubMed 21968188PubMed 21988832PubMed 23455922PubMed 23555304. Source: IntAct

protein domain specific binding

Inferred from physical interaction PubMed 11984006. Source: UniProtKB

protein kinase regulator activity

Non-traceable author statement Ref.1. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 19233263PubMed 19592636. Source: BHF-UCL

transcription factor binding

Inferred from physical interaction PubMed 19324893. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 215214Casein kinase II subunit beta
PRO_0000068236

Regions

Region188 – 1936Interaction with alpha subunit By similarity
Compositional bias55 – 6410Asp/Glu-rich (acidic)

Sites

Metal binding1091Zinc
Metal binding1141Zinc
Metal binding1371Zinc
Metal binding1401Zinc

Amino acid modifications

Modified residue21N-acetylserine
Modified residue21Phosphoserine; by autocatalysis Ref.28
Modified residue31Phosphoserine; by autocatalysis Ref.28
Modified residue2091Phosphoserine Ref.20 Ref.22 Ref.24 Ref.26
Modified residue2121N6-acetyllysine Ref.23

Experimental info

Sequence conflict1941P → A in AAA52123. Ref.3

Secondary structure

.............................................. 215
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P67870 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: E465B1E699B0E0EC

FASTA21524,942
        10         20         30         40         50         60 
MSSSEEVSWI SWFCGLRGNE FFCEVDEDYI QDKFNLTGLN EQVPHYRQAL DMILDLEPDE 

        70         80         90        100        110        120 
ELEDNPNQSD LIEQAAEMLY GLIHARYILT NRGIAQMLEK YQQGDFGYCP RVYCENQPML 

       130        140        150        160        170        180 
PIGLSDIPGE AMVKLYCPKC MDVYTPKSSR HHHTDGAYFG TGFPHMLFMV HPEYRPKRPA 

       190        200        210 
NQFVPRLYGF KIHPMAYQLQ LQAASNFKSP VKTIR 

« Hide

References

« Hide 'large scale' references
[1]"Human phosvitin/casein kinase type II. Molecular cloning and sequencing of full-length cDNA encoding subunit beta."
Jakobi R., Voss H., Pyerin W.
Eur. J. Biochem. 183:227-233(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Expression of the cDNA for the beta subunit of human casein kinase II confers partial UV resistance on xeroderma pigmentosum cells."
Teitz T., Eli D., Penner M., Bakhanashvili M., Naiman T., Timme T.L., Wood C.M., Moses R.E., Canaani D.
Mutat. Res. 236:85-97(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning and characterization of a cDNA encoding the beta subunit of human casein kinase II."
Heller-Harrison R.A., Meisner H., Czech M.P.
Biochemistry 28:9053-9058(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Structure of the gene encoding human casein kinase II subunit beta."
Voss A., Wirkner U., Jacobi R., Hewitt N., Schwager C., Zimmermann J., Ansorge W., Pyerin W.
J. Biol. Chem. 266:13706-13711(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Sequencing of full-length cDNA encoding the alpha and beta subunits of human casein kinase II from human platelets and megakaryocytic cells. Expression of the casein kinase IIalpha intronless gene in a megakaryocytic cell line."
Singh L.S., Kalafatis M.
Biochemistry 41:8935-8940(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
Shiina S., Tamiya G., Oka A., Inoko H.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[10]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[11]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[14]"Stimulation of casein kinase II by epidermal growth factor: relationship between the physiological activity of the kinase and the phosphorylation state of its beta subunit."
Ackerman P., Glover C.V., Osheroff N.
Proc. Natl. Acad. Sci. U.S.A. 87:821-825(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[15]"Interaction of CD163 with the regulatory subunit of casein kinase II (CKII) and dependence of CD163 signaling on CKII and protein kinase C."
Ritter M., Buechler C., Kapinsky M., Schmitz G.
Eur. J. Immunol. 31:999-1009(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CD163.
[16]"A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1."
Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H., Goodman R., Lozano G., Zhao Y., Lu H.
Mol. Cell 7:283-292(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SSRP1 AND SUPT16H.
[17]"Identification of ribosome-binding protein p34 as an intracellular protein that binds acidic fibroblast growth factor."
Skjerpen C.S., Wesche J., Olsnes S.
J. Biol. Chem. 277:23864-23871(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FGF1.
[18]"p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex."
Keller D.M., Lu H.
J. Biol. Chem. 277:50206-50213(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SSRP1 AND SUPT16H.
[19]"Casein kinase 2-dependent serine phosphorylation of MuSK regulates acetylcholine receptor aggregation at the neuromuscular junction."
Cheusova T., Khan M.A., Schubert S.W., Gavin A.C., Buchou T., Jacob G., Sticht H., Allende J., Boldyreff B., Brenner H.R., Hashemolhosseini S.
Genes Dev. 20:1800-1816(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF MUSK, INTERACTION WITH MUSK.
[20]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"Crystal structure of the human protein kinase CK2 regulatory subunit reveals its zinc finger-mediated dimerization."
Chantalat L., Leroy D., Filhol O., Nueda A., Benitez M.J., Chambaz E.M., Cochet C., Dideberg O.
EMBO J. 18:2930-2940(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 1-182, SUBUNIT, ZINC-BINDING SITES.
[28]"Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme."
Niefind K., Guerra B., Ermakowa I., Issinger O.G.
EMBO J. 20:5320-5331(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CSNK2A1, ZINC-BINDING SITES, SUBUNIT, PHOSPHORYLATION AT SER-2 AND SER-3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16937 mRNA. Translation: CAA34811.1.
X16312 mRNA. Translation: CAA34379.1.
M30448 mRNA. Translation: AAA52123.1.
X57152 Genomic DNA. Translation: CAA40442.1.
AY113186 mRNA. Translation: AAM50092.1.
CR541699 mRNA. Translation: CAG46500.1.
AF129756 Genomic DNA. Translation: AAD18081.1.
BA000025 Genomic DNA. Translation: BAB63386.1.
DQ314868 Genomic DNA. Translation: ABC40727.1.
AK311860 mRNA. Translation: BAG34801.1.
AL662899 Genomic DNA. Translation: CAI96141.1.
AL662899 Genomic DNA. Translation: CAI18393.2. Different initiation.
AL670886 Genomic DNA. Translation: CAI17800.1.
AL805934 Genomic DNA. Translation: CAI18523.1.
BX511262 Genomic DNA. Translation: CAM45825.1.
CR753842 Genomic DNA. Translation: CAQ06572.1.
CR354443 Genomic DNA. Translation: CAQ07002.1.
CR759761 Genomic DNA. Translation: CAQ10879.1.
CH471081 Genomic DNA. Translation: EAX03473.1.
BC112017 mRNA. Translation: AAI12018.1.
BC112019 mRNA. Translation: AAI12020.1.
CCDSCCDS4712.1.
PIRA39459.
RefSeqNP_001269314.1. NM_001282385.1.
NP_001311.3. NM_001320.6.
UniGeneHs.73527.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DS5X-ray3.16E/F/G/H181-203[»]
1JWHX-ray3.10C/D1-215[»]
1QF8X-ray1.74A/B1-182[»]
3EEDX-ray2.80A/B1-193[»]
4DGLX-ray3.00A/B1-215[»]
4MD7X-ray3.10A/B/C/D1-215[»]
4MD8X-ray3.30A/B/C/D1-215[»]
4MD9X-ray3.50A/B/C/D/I/J/N/O1-215[»]
4NH1X-ray3.30C/D1-215[»]
ProteinModelPortalP67870.
SMRP67870. Positions 7-207.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107843. 212 interactions.
DIPDIP-131N.
IntActP67870. 178 interactions.
MINTMINT-88683.
STRING9606.ENSP00000415615.

Chemistry

BindingDBP67870.
ChEMBLCHEMBL2358.

Polymorphism databases

DMDM54037520.

Proteomic databases

MaxQBP67870.
PaxDbP67870.
PRIDEP67870.

Protocols and materials databases

DNASU1460.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375865; ENSP00000365025; ENSG00000204435.
ENST00000375866; ENSP00000365026; ENSG00000204435.
ENST00000375882; ENSP00000365042; ENSG00000204435.
ENST00000383427; ENSP00000372919; ENSG00000206406.
ENST00000383433; ENSP00000372925; ENSG00000206406.
ENST00000400110; ENSP00000382980; ENSG00000206406.
ENST00000412802; ENSP00000413469; ENSG00000224774.
ENST00000418230; ENSP00000411322; ENSG00000228875.
ENST00000422567; ENSP00000407018; ENSG00000224398.
ENST00000429633; ENSP00000409510; ENSG00000230700.
ENST00000431476; ENSP00000394855; ENSG00000224398.
ENST00000436169; ENSP00000412520; ENSG00000224398.
ENST00000443673; ENSP00000400188; ENSG00000230700.
ENST00000448596; ENSP00000391038; ENSG00000232960.
ENST00000451917; ENSP00000415303; ENSG00000224774.
ENST00000452985; ENSP00000415237; ENSG00000228875.
ENST00000453234; ENSP00000395275; ENSG00000224774.
ENST00000454382; ENSP00000390900; ENSG00000232960.
ENST00000454511; ENSP00000393756; ENSG00000232960.
ENST00000455161; ENSP00000407379; ENSG00000230700.
ENST00000458330; ENSP00000410802; ENSG00000228875.
GeneID1460.
KEGGhsa:1460.
UCSCuc003nvr.1. human.

Organism-specific databases

CTD1460.
GeneCardsGC06P031633.
GC06Pj31620.
GC06Pk31615.
GC06Pl31672.
GC06Pm31709.
GC06Pn31623.
GC06Po31622.
HGNCHGNC:2460. CSNK2B.
HPACAB004349.
CAB013087.
CAB016059.
HPA005944.
MIM115441. gene.
neXtProtNX_P67870.
PharmGKBPA26960.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5041.
HOGENOMHOG000039270.
HOVERGENHBG051131.
InParanoidP67870.
KOK03115.
PhylomeDBP67870.
TreeFamTF314462.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
SignaLinkP67870.

Gene expression databases

BgeeP67870.
CleanExHS_CSNK2B.
GenevestigatorP67870.

Family and domain databases

Gene3D1.10.1820.10. 1 hit.
2.20.25.20. 1 hit.
InterProIPR016149. Casein_kin_II_reg-sub_a-hlx.
IPR016150. Casein_kin_II_reg-sub_b-sht.
IPR000704. Casein_kinase_II_reg-sub.
[Graphical view]
PANTHERPTHR11740. PTHR11740. 1 hit.
PfamPF01214. CK_II_beta. 1 hit.
[Graphical view]
PRINTSPR00472. CASNKINASEII.
SMARTSM01085. CK_II_beta. 1 hit.
[Graphical view]
SUPFAMSSF57798. SSF57798. 1 hit.
PROSITEPS01101. CK2_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP67870.
GeneWikiCSNK2B.
GenomeRNAi1460.
NextBio6001.
PROP67870.
SOURCESearch...

Entry information

Entry nameCSK2B_HUMAN
AccessionPrimary (citable) accession number: P67870
Secondary accession number(s): B0UXA9 expand/collapse secondary AC list , P07312, P13862, Q4VX47
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: July 9, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM